1ag4

<StructureSection load='1ag4' size='340' side='right'caption='[[1ag4]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1ag4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Phypo Phypo]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AG4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AG4 FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ag4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ag4 OCA], [https://pdbe.org/1ag4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ag4 RCSB], [https://www.ebi.ac.uk/pdbsum/1ag4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ag4 ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/SR3A_PHYPO SR3A_PHYPO]] Structural protein.

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== Publication Abstract from PubMed ==

Spherulin 3a is the most abundantly expressed cytosolic protein in spherulating plasmodia of the slime mold Physarum polycephalum. High yields of unlabeled, uniformly 15N and uniformly 13C/15N-labeled recombinant spherulin 3a from Escherichia coli could be produced by a simple protocol described here. The three-dimensional solution structure of Ca2+-loaded spherulin 3a was determined by homo- and heteronuclear NMR spectroscopy. The structure of monomeric spherulin 3a consists of two pleated beta-sheets plus a short alpha-helix arranged into the gamma-crystallin fold. The beta-sheets comprise two intertwined Greek-key motifs. An additional N-terminal beta-strand is unique to spherulin 3a. Complexation of calcium ions greatly enhances overall conformational stability of the protein. The average atomic root-mean-square deviations (r.m.s.d.) for heavy atoms in beta-strands were 0.34(+/-0.16) A for the backbone atoms and 0.73(+/-0.40) A for all atoms. The corresponding r.m.s.d. values for heavy atoms in the whole protein were 0.62(+/-0.42) A for the backbone atoms and 0.99(+/-0.65) A for all atoms. We show the structural relationship between spherulin 3a, a myxomycete dormancy protein, and crystallins from the vertebrate eye lens. Since spherulin 3a has a structure corresponding to one domain of bovine gammaB(II)-crystallin, it represents a hypothetical ancestral gamma-crystallin precursor structure.

Ca2+-loaded spherulin 3a from Physarum polycephalum adopts the prototype gamma-crystallin fold in aqueous solution.,Rosinke B, Renner C, Mayr EM, Jaenicke R, Holak TA J Mol Biol. 1997 Aug 29;271(4):645-55. PMID:9281431<ref>PMID:9281431</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1ag4" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Phypo]]

[[Category: Holak, T A]]

[[Category: Jaenicke, R]]

[[Category: Mayr, E M]]

[[Category: Renner, C]]

[[Category: Rosinke, B]]

[[Category: Structural protein]]